VP44_BPAPS
ID VP44_BPAPS Reviewed; 93 AA.
AC Q9T1Q4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Putative nuclease p44;
DE EC=3.1.-.-;
GN Name=44;
OS Acyrthosiphon pisum secondary endosymbiont phage 1 (Bacteriophage APSE-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Sendosyvirus.
OX NCBI_TaxID=2682836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10489345; DOI=10.1006/viro.1999.9902;
RA van der Wilk F., Dullemans A.M., Verbeek M., van den Heuvel J.F.J.M.;
RT "Isolation and characterization of APSE-1, a bacteriophage infecting the
RT secondary endosymbiont of acyrthosiphon pisum.";
RL Virology 262:104-113(1999).
CC -!- FUNCTION: Nuclease. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Mg(2+) is the most probable.
CC {ECO:0000250};
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DR EMBL; AF157835; AAF03987.1; -; Genomic_DNA.
DR RefSeq; NP_051005.1; NC_000935.1.
DR SMR; Q9T1Q4; -.
DR GeneID; 1262338; -.
DR KEGG; vg:1262338; -.
DR Proteomes; UP000000853; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR SMART; SM00990; VRR_NUC; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..93
FT /note="Putative nuclease p44"
FT /id="PRO_0000077871"
FT DOMAIN 5..84
FT /note="VRR-NUC"
SQ SEQUENCE 93 AA; 10356 MW; B7EEE57CB8BB3C63 CRC64;
MRLIREDSIE KHLVSEVRKI GGIAYKFVSP GRRGVPDRLV ALPNGKIIFV ECKAPGEKPT
PYQLREHARL FALGHQVIVL DSQDLSSILP AVN